about
Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicityNatural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formationHuman metallothioneins 2 and 3 differentially affect amyloid-beta binding by transthyretinIodination of salicylic acid improves its binding to transthyretinIodine Atoms: A New Molecular Feature for the Design of Potent Transthyretin Fibrillogenesis InhibitorsEpigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: "in vivo" evidence from FAP mice modelsMolecular Tweezers Targeting Transthyretin AmyloidosisSubstrate specificity of transthyretin: identification of natural substrates in the nervous system.Functional characterization of Arabidopsis thaliana transthyretin-like protein.Tuning transthyretin amyloidosis inhibition properties of iododiflunisal by combinatorial engineering of the nonsalicylic ring substitutions.Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.Curcumin: A multi-target disease-modifying agent for late-stage transthyretin amyloidosis.Clearance of extracellular misfolded proteins in systemic amyloidosis: experience with transthyretin.Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design.Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation.Gene therapy approach to FAP: in vivo influence of T119M in TTR deposition in a transgenic V30M mouse model.Selective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative.Isatin derivatives, a novel class of transthyretin fibrillogenesis inhibitors.Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of Familial Amyloidotic Polyneuropathy.Transthyretin chemical chaperoning by flavonoids: Structure-activity insights towards the design of potent amyloidosis inhibitors.The binding of xanthone derivatives to transthyretin.Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model.Impairment of autophagy by TTR V30M aggregates: in vivo reversal by TUDCA and curcumin.Natural polyphenols as modulators of TTR amyloidogenesis:in vitroandin vivoevidences towards therapyTTR Leu 64 in an FAP kindred identified by PCR-RFLP analysisDietary curcumin counteracts extracellular transthyretin deposition: Insights on the mechanism of amyloid inhibitionComparative Studies of Two Transthyretin Variants with Protective Effects on Familial Amyloidotic Polyneuropathy: TTR R104H and TTR T119MHaplotype analysis of common transthyretin mutationsTransthyretin Leu 68 in a form of cardiac amyloidosisFamilial amyloidotic polyneuropathy: transthyretin (prealbumin) variants in kindreds of Italian originTTR exon scanning in peripheral neuropathiesUncovering the Neuroprotective Mechanisms of Curcumin on Transthyretin AmyloidosisScreening and biochemical characterization of transthyretin variants in the Portuguese populationTargeting transthyretin amyloidosis in the eye with next-generation stabilizers: AT40 displays potent TTR stabilization in the human vitreous
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P50
description
researcher ORCID ID = 0000-0001-9289-3835
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wetenschapper
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name
Maria Rosário Almeida
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Maria Rosário Almeida
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Maria Rosário Almeida
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Maria Rosário Almeida
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type
label
Maria Rosário Almeida
@ast
Maria Rosário Almeida
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Maria Rosário Almeida
@es
Maria Rosário Almeida
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prefLabel
Maria Rosário Almeida
@ast
Maria Rosário Almeida
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Maria Rosário Almeida
@es
Maria Rosário Almeida
@nl
P106
P1153
57190193603
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0000-0001-9289-3835